Carbon nanotubes as nanovectors for intracellular delivery of laronidase in Mucopolysaccaridosis type I

Abstract

The immobilization of proteins on carbon nanotubes (CNTs) has been widely reported mainly for the preparation of sensors while the conjugation of enzymes for therapeutic purposes has been scarcely considered. Herein we report, at the best of our knowledge, the first example of intracellular delivery of a therapeutic enzyme by means of CNTs, retaining its activity. Mucopolisaccharodosis I is a rare genetic disease characterized by a deficiency or absence of activity of the α-L-iduronidase (IDUA) enzyme. We evaluated the capacity of the recombinant form of human IDUA enzyme, laronidase (Aldurazyme®), conjugated with CNTs to be internalized by fibroblasts from subjects affected with Mucopolisaccaridosis type I and the capacity of the enzyme to keep its activity after internalization. The enzyme was successfully delivered into the lysosomal space and the enzymatic activity of the conjugate was preserved after internalization up to 48 hours. This paves the way towards the use of such kind of constructs for therapeutic applications.

Authors contributing to RSC publications (journal articles, books or book chapters)
do not need to formally request permission to reproduce material contained in this
article provided that the correct acknowledgement is given with the reproduced material.

Reproduced material should be attributed as follows:

For reproduction of material from NJC:
Reproduced from Ref. XX with permission from the Centre National de la Recherche
Scientifique (CNRS) and The Royal Society of Chemistry.

For reproduction of material from PCCP:
Reproduced from Ref. XX with permission from the PCCP Owner Societies.

For reproduction of material from PPS:
Reproduced from Ref. XX with permission from the European Society for Photobiology,
the European Photochemistry Association, and The Royal Society of Chemistry.

For reproduction of material from all other RSC journals and books:
Reproduced from Ref. XX with permission from The Royal Society of Chemistry.

If the material has been adapted instead of reproduced from the original RSC publication
"Reproduced from" can be substituted with "Adapted from".

In all cases the Ref. XX is the XXth reference in the list of references.

If you are the author of this article you do not need to formally request permission
to reproduce figures, diagrams etc. contained in this article in third party publications
or in a thesis or dissertation provided that the correct acknowledgement is given
with the reproduced material.

Reproduced material should be attributed as follows:

For reproduction of material from NJC:
[Original citation] - Reproduced by permission of The Royal Society of Chemistry (RSC) on behalf of the
Centre National de la Recherche Scientifique (CNRS) and the RSC

For reproduction of material from PCCP:
[Original citation] - Reproduced by permission of the PCCP Owner Societies

For reproduction of material from PPS:
[Original citation] - Reproduced by permission of The Royal Society of Chemistry (RSC) on behalf of the
European Society for Photobiology, the European Photochemistry Association, and
RSC

For reproduction of material from all other RSC journals:
[Original citation] - Reproduced by permission of The Royal Society of Chemistry

If you are the author of this article you still need to obtain permission to reproduce
the whole article in a third party publication with the exception of reproduction
of the whole article in a thesis or dissertation.

Information about reproducing material from RSC articles with different licences
is available on our Permission Requests page.